This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pierce, J. S. Articles by Strauss, J. H. Search for Related Content PubMed PubMed Citation Articles by Pierce, J. S. Articles by Strauss, J. H.

 Previous Article  |  Next Article 

J Virol. 1974 May; 13(5): 1030-1036
Copyright © 1974 American Society for Microbiology. All Rights Reserved.

Effect of Ionic Strength on the Binding of Sindbis Virus to Chick Cells

^a Division of Biology, California Institute of Technology, Pasadena, California 91109

ABSTRACT

Sindbis virus can adsorb to chicken embryo fibroblasts in two different ways. "Loosely" bound virus can be washed off the cell with buffers of ionic strength 0.2 or greater, whereas "tightly" bound virus remains attached under these conditions. When Sindbis virus is adsorbed to chick cells at 4 C from a buffer of ionic strength 0.17, 40 to 50% of the adsorbed virus is loosely bound, the remainder tightly bound. Infection of chick cells by Sindbis virus has only small effects on the total amount of virus that can be bound to the cells. However, the amount of Sindbis virus that can be tightly bound declines rapidly beginning at 2 to 3 h after infection. By 7 h after infection, the amount of virus that can be tightly bound is only 10 to 20% of the amount bound to uninfected cells. The adsorption (and penetration) of virus at 37 C is most efficient at an ionic strength of 0.15 to 0.17; at this ionic strength most of the adsorbed virus is tightly bound. At higher ionic strengths the virus adsorbs poorly. At lower ionic strengths most of the virus is loosely bound. A second enveloped virus, vesicular stomatitis virus, has been studied for the purposes of comparison; its adsorption behavior differs from that of Sindbis virus.

¹ Present address: Department of Microbiology, University of Illinois at the Medical Center, Chicago, Ill. 60680.

This article has been cited by other articles:

• Bick, M. J., Carroll, J.-W. N., Gao, G., Goff, S. P., Rice, C. M., MacDonald, M. R. (2003). Expression of the Zinc-Finger Antiviral Protein Inhibits Alphavirus Replication. J. Virol. 77: 11555-11562 [Abstract] [Full Text]  
• Kim, K. H., Strauss, E. G., Strauss, J. H. (2000). Adaptive Mutations in Sindbis Virus E2 and Ross River Virus E1 That Allow Efficient Budding of Chimeric Viruses. J. Virol. 74: 2663-2670 [Abstract] [Full Text]  
• Frolov, I., Agapov, E., Hoffman, T. A. Jr., Prágai, B. M., Lippa, M., Schlesinger, S., Rice, C. M. (1999). Selection of RNA Replicons Capable of Persistent Noncytopathic Replication in Mammalian Cells. J. Virol. 73: 3854-3865 [Abstract] [Full Text]  
• Byrnes, A. P., Griffin, D. E. (1998). Binding of Sindbis Virus to Cell Surface Heparan Sulfate. J. Virol. 72: 7349-7356 [Abstract] [Full Text]  
• Klimstra, W. B., Ryman, K. D., Johnston, R. E. (1998). Adaptation of Sindbis Virus to BHK Cells Selects for Use of Heparan Sulfate as an Attachment Receptor. J. Virol. 72: 7357-7366 [Abstract] [Full Text]  
• Yao, J., Strauss, E. G., Strauss, J. H. (1998). Molecular Genetic Study of the Interaction of Sindbis Virus E2 with Ross River Virus E1 for Virus Budding. J. Virol. 72: 1418-1423 [Abstract] [Full Text]